Date published: 2026-2-15

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cathepsin 8 Activators

Cathepsin 8, a member of the cysteine protease family localized within lysosomes, is a key regulator of cellular proteolysis and immune responses. Within the acidic environment of lysosomes, cathepsin 8 plays a pivotal role in cleaving a diverse range of substrates, contributing to protein turnover, cellular homeostasis, and antigen presentation. As a lysosomal cysteine protease, cathepsin 8 is primarily involved in the degradation of endocytosed proteins, ensuring the turnover of cellular components. Its role extends beyond mere proteolysis, as cathepsin 8 is actively implicated in antigen processing, playing a crucial part in the adaptive immune system. By cleaving antigenic peptides within lysosomes, cathepsin 8 contributes to the generation of major histocompatibility complex class II (MHC-II) peptides, a pivotal step in presenting antigens to immune cells. This function underscores cathepsin 8's significance in shaping immune responses and cellular surveillance.

The activation of cathepsin 8 involves a sophisticated interplay of direct and indirect mechanisms that modulate its enzymatic activity and stability. Direct activators, such as specific inhibitors like E64d and Leupeptin, act by preventing the degradation of cathepsin 8, thereby maintaining its stability and enzymatic function within lysosomes. Indirect activators, exemplified by compounds like Rapamycin or NH4Cl, influence cathepsin 8 activation by engaging broader cellular pathways. For instance, Rapamycin indirectly stimulates cathepsin 8 by activating the mTORC1 pathway, subsequently enhancing lysosomal biogenesis and cathepsin 8 expression. Additionally, NH4Cl, by altering lysosomal pH, indirectly activates cathepsin 8, illustrating the intricate regulation of its activity within the lysosomal environment. This combination of direct and indirect activation mechanisms highlights the nuanced control of cathepsin 8, emphasizing its essential role in cellular processes ranging from proteolysis to immune regulation.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Rapamycin

53123-88-9sc-3504
sc-3504A
sc-3504B
1 mg
5 mg
25 mg
$63.00
$158.00
$326.00
233
(4)

Rapamycin indirectly stimulates cathepsin 8 by activating the mTORC1 pathway. By inhibiting mTORC1, Rapamycin induces autophagy, leading to increased lysosomal biogenesis and cathepsin 8 expression. This indirect activation contributes to enhanced lysosomal degradation, illustrating how Rapamycin influences cathepsin 8 through the mTORC1-autophagy axis.

FCM Lysing solution (1x)

sc-3621
150 ml
$62.00
8
(1)

This solution indirectly activates cathepsin 8 by raising lysosomal pH. By inhibiting the vacuolar-type H+-ATPase, NH4Cl prevents lysosomal acidification, promoting cathepsin 8 activity. This indirect activation enhances lysosomal degradation processes, illustrating how NH4Cl influences cathepsin 8 through modulating lysosomal pH.

Bafilomycin A1

88899-55-2sc-201550
sc-201550A
sc-201550B
sc-201550C
100 µg
1 mg
5 mg
10 mg
$98.00
$255.00
$765.00
$1457.00
280
(6)

Bafilomycin A1 indirectly activates cathepsin 8 by inhibiting the vacuolar-type H+-ATPase. By preventing lysosomal acidification, Bafilomycin A1 promotes cathepsin 8 activity. This indirect activation enhances lysosomal degradation processes, illustrating how Bafilomycin A1 influences cathepsin 8 through modulating lysosomal pH.

Concanamycin A

80890-47-7sc-202111
sc-202111A
sc-202111B
sc-202111C
50 µg
200 µg
1 mg
5 mg
$66.00
$167.00
$673.00
$2601.00
109
(2)

Concanamycin A indirectly stimulates cathepsin 8 by inhibiting the vacuolar-type H+-ATPase. By preventing lysosomal acidification, Concanamycin A promotes cathepsin 8 activity. This indirect activation contributes to increased lysosomal degradation processes, illustrating how Concanamycin A influences cathepsin 8 through modulating lysosomal pH.